Decreasing foulant deposition on at least one surface by contacting the surface(s) with at least one protein

ABSTRACT

Corrosion and/or calcium scale deposition on a surface in contact with corrosion forming components and/or scale forming components within a subterranean formation may be decreased, prevented, and/or inhibited by contacting the surface with at least one protein. The protein(s) may be or include, but is not limited to, at least one aspein protein, at least one aspolin protein, at least one dentine protein, at least one DRICH-1 protein, at least one nacrein protein, at least one SMDT-1 protein, derivatives thereof, fragments thereof, mimetics thereof, and combinations thereof. The surface may be or include, but is not limited to a metal surface, a plastic surface, a ceramic surface, a painted surface, a coated surface, and combinations thereof.

CROSS-REFERENCE TO RELATED APPLICATION

This application is a divisional application of U.S. Ser. No. 15/266,436filed Sep. 15, 2016, issued as U.S. Pat. No. 10,196,554 on Feb. 5, 2019,that in turn claims the benefit of Provisional Patent Application No.62/237,808 filed Oct. 6, 2015, both of which are incorporated byreference herein in their entireties.

TECHNICAL FIELD

The present invention relates to decreasing foulant formation and/orfoulant deposition on at least one surface by contacting the surface(s)with at least one protein, such as but not limited to at least oneaspein protein, at least one aspolin protein, at least one dentineprotein, at least one DRICH-1 protein, at least one nacrein protein, atleast one SMDT-1 protein, derivatives thereof, fragments thereof,mimetics thereof, and combinations thereof.

BACKGROUND

The problems of foulant formation and/or foulant deposition havetroubled downhole operations for years. Foulants accumulate on internalwalls of various water systems, pipe surfaces, wellbore surfaces, etc.and thereby materially lessen the operational efficiency of a downholeoperation.

Much of the foulant formation and/or foulant deposition occurs as aresult of various components added to a fluid for various reasons, suchas the salt for brine-based fluids, corrosion inhibition, bridgingagents, scale inhibitors, and the like. The foulants may be or includescale, corrosion, and combinations thereof. The various corrosionforming components may cause corrosion to a downhole surface. Thevarious scale forming components may precipitate from the fluid asscale, and it is this formed scale that may deposit onto a surface,which may occur at each instance of scale formation.

For example, corrosion may occur and/or scale may form because abrine-based fluid or system becomes saturated with a material due to achange in the flowing fluid conditions within the subterraneanformation. Formation of corrosion and/or scale may occur when mixinginsoluble waters, out-gassing, shear, turbulence, temperature and/orpressure changes, and combinations thereof; from pressure drops, watermixing points, outgassing points, shear points, gravel packs, and thelike.

Chemical corrosion inhibitors decrease the amount and/or rate ofcorrosion formation and thereby decrease the amount of corrosion to adownhole surface. Chemical scale inhibitors decrease the amount and/orrate of scale formation in and around the surfaces within a subterraneanformation, such as a subterranean reservoir wellbore.

Traditional inhibitors, such as ion exchange resins, polyacrylic acids,and the like are used as anti-foulants against scale and/or corrosionforming components. But such anti-foulants are extremely toxic, andother traditional inhibitors for decreasing corrosion and/or scale havenot been satisfactory in an environment having a high amount of scaleforming components, corrosion forming components, and/or a high amountof total dissolved solids.

For this reason, polyaspartic acid has been used for decreasing scaleand/or corrosion on surfaces within a subterranean reservoir wellboreand/or surface in a refinery (e.g. an oil/gas refinery). However,polyaspartic acid is difficult to manufacture in large quantities. Inaddition, polyaspartic acid contains 50% alpha structures and 50% betastructures, but only the alpha structures are effective in decreasingformation and/or deposition of scale forming components and/or corrosionforming components onto a surface.

Thus, it would be desirable to determine other useful proteins fordecreasing foulant formation and/or foulant deposition, but where theproteins are easily reproducible on a large scale.

SUMMARY

There is provided, in one form, an additive composition for a basefluid, such as but not limited to, a drilling fluid, a completion fluid,a production fluid, a servicing fluid, an injection fluid, a refineryfluid, and combinations thereof. The additive composition may include atleast one protein, such as but not limited to, at least one aspeinprotein, at least one aspolin protein, at least one dentine protein, atleast one DRICH-1 protein, at least one nacrein protein, at least oneSMDT-1 protein, derivatives thereof, fragments thereof, mimeticsthereof, and combinations thereof.

There is further provided in another non-limiting embodiment, a fluidcomposition including a base fluid, at least one protein, and at leastone foulant forming component where less foulant formation occurs in thepresence of the at least one protein as compared to an otherwiseidentical fluid composition absent the at least one protein. The basefluid may be or include, but is not limited to, aqueous-based fluids,non-aqueous-based fluids, emulsified fluids, non-emulsified fluids, andcombinations thereof. The protein(s) may be or include, but is notlimited to at least one aspein protein, at least one aspolin protein, atleast one dentine protein, at least one DRICH-1 protein, at least onenacrein protein, an SMDT-1 protein, derivatives thereof, fragmentsthereof, mimetics thereof, and combinations thereof.

In another non-limiting embodiment, a method may include contacting atleast one surface with at least one protein, and decreasing an amount offoulant deposition onto the surface as compared to an otherwiseidentical surface absent the contact of the surface with the at leastone protein. The protein(s) may be or include, but are not limited to,at least one aspein protein, at least one aspolin protein, at least onedentine protein, at least one DRICH-1 protein, at least one nacreinprotein, at least one SMDT-1 protein, derivatives thereof, fragmentsthereof, mimetics thereof, and combinations thereof.

BRIEF DESCRIPTION OF THE DRAWINGS

In order to more fully understand the drawings referred to in thedetailed description, a brief description of each drawing is presentedhere:

FIG. 1 (SEQ ID NO:1) represents the amino acid sequence of an aspeinprotein;

FIG. 2 (SEQ ID NO:2) represents the amino acid sequence of an aspolin 1protein;

FIG. 3 (SEQ ID NO:3) represents the amino acid sequence of an aspolin 2protein; and

FIG. 4 represents a pGS21 plasmid for use as an expression vector for atleast one recombinant protein(s).

DETAILED DESCRIPTION

It has been discovered that an additive composition may help to decreasefoulant formation within a base fluid and/or decrease foulant depositionon at least one surface as compared to an otherwise identical base fluidand/or surface absent the contact with the additive composition and/orfluid composition. The additive composition may include at least oneprotein having an amino acid sequence of at least 60% aspartic acid,such as but not limited to, at least one aspein protein, at least oneaspolin protein, at least one dentine protein, at least one DRICH-1protein (also known as an aspartate rich protein), at least one nacreinprotein, at least one SMDT-1 protein (also known as a single passmembrane protein with an aspartate rich tail), derivatives thereof,fragments thereof, mimetics thereof, and combinations thereof.

The protein(s) may be less toxic to the environment, as compared toconventional non-biodegradable anti-foulants used for the same purpose,and the protein(s) may be made from renewable resources. The use of theprotein(s) in a base fluid may provide a renewable alternative toconventional additives (non-biodegradable) that are used to decreasefoulant deposition to a surface and/or foulant formation within a basefluid. In addition, the protein(s) may have an amino acid sequencecomprising where a majority of the amino acid sequence is aspartic acid.

In a non-limiting embodiment, the aspein protein may be or include anaspein protein having an amino acid sequence at least 75% homologous tothe amino acid sequence of SEQ ID NO:1. In a non-limiting embodiment,the aspolin protein may be or include an aspolin protein I having anamino acid sequence at least 75% homologous to the amino acid sequenceof SEQ ID NO:2. In a non-limiting embodiment, the aspolin protein may beor include an aspolin protein II having an amino acid sequence at least75% homologous to the amino acid sequence of SEQ ID NO:3.

‘Derived from’ with respect to the protein(s) is meant to include wholeproteins or protein fragments, and/or where the protein originated froma particular species and was isolated from that particular species;‘derived from’ also encompasses polypeptides identical in amino acidsequence to the active site of the particular protein that isrecombinantly expressed in a host cell expression system or chemicallysynthesized. ‘Recombinant DNA’ is DNA that has been formed artificiallyby combining constituents from different organisms, such as insertingthe gene sequence into an E. coli host cell for expression of the targetprotein in a non-limiting example.

For example, the aspein protein having the amino acid sequence of FIG. 1(SEQ ID NO:1) may be derived from Pinctada fucata, a type of pearloyster or recombinant protein is expressed from the cDNA encoding theprotein. The aspolin protein(s) having the amino acid sequence of FIG. 2(SEQ ID NO:2) and/or FIG. 3 (SEQ ID NO:3) may be derived from a WallEyePollack, a type of fish or recombinant protein is expressed from thecDNA encoding the protein.

‘Derived from’ also includes derivatives of the proteins, such as apolypeptide or fragment that may be substantially similar in primarystructural sequence to the protein(s) described herein, but which mayinclude chemical and/or biochemical modifications that are not found inthe native polypeptide. Such chemical and/or biochemical modificationsare discussed in more detail below.

The primary structural sequence is the sequence of amino acids linkedtogether to form the primary structure of for the protein(s). Thesecondary structure of the protein refers to the pairing interactionsbetween the amino acids within a single protein or set of interactingmolecules therein, such as a beta-helix in the protein. Tertiarystructure refers to the three-dimensional structure of the proteinformed from the amino acid sequence. Quaternary structure refers to theinteraction between at least two tertiary structures.

‘Fragment’ as used herein is meant to include any amino acid sequenceshorter than the full-length protein(s), but where the fragmentmaintains similar activity to the full-length protein(s). Fragments mayinclude a single contiguous sequence identical to a portion of theprotein sequence. Alternatively, the fragment may have or includeseveral different shorter segments where each segment is identical inamino acid sequence to a different portion of the amino acid sequence ofthe protein(s), but linked via amino acids differing in sequence fromthe protein(s). ‘Mimetic’ as used herein may include polypeptides, whichmay be recombinant, and peptidomimetics, as well as small organicmolecules, which exhibit similar or enhanced activity as compared to theprotein(s) described herein.

The translated amino acid sequence for at least one protein may besubstantially homologous to the amino acid sequence of FIG. 1 (SEQ IDNO:1), FIG. 2 (SEQ ID NO:2), or FIG. 3 (SEQ ID NO:3) in a non-limitingembodiment. The term “substantially homologous” is used herein to denotean amino acid sequence having at least 75% sequence identity to thesequences shown in FIG. 1 (SEQ ID NO:1), FIG. 2 (SEQ ID NO:2), or FIG. 3(SEQ ID NO:3), alternatively from about 80% independently to about99.5%, or from about 85% independently to about 95%. As used herein withrespect to a range, “independently” means that any threshold may be usedtogether with another threshold to give a suitable alternative range,e.g. about 75% independently to about 85% is also considered a suitablealternative range.

In a non-limiting embodiment, the non-limiting isolated protein(s) issubstantially free of other proteins. The non-limiting protein(s) may bein a form that is at least 40% pure, alternatively from about 60% pureindependently to about 99.5% pure, or from about 75% pure independentlyto about 90% pure as determined by SDS-PAGE.

In another non-limiting embodiment, the protein(s) may have at least oneglycosylation site. The glycosylation site(s) may aid the protein(s) indecreasing/preventing/inhibiting foulant formation and/or foulantdeposition. The glycosylation sites may be present in the primarystructure of the protein. Glycosylation between a carbohydrate, i.e. aglycosyl donor, is attached to a hydroxyl or other functional group ofanother molecule, i.e. a glycosyl acceptor. Glycosylation refers to anenzymatic process where glycans may attach to proteins, lipids, or otherorganic molecules. Glycosylation is a form of co-translational andpost-translational modification.

‘Deposited’ as used herein means that the foulant forming components atleast partially form a layer onto the surface either by absorbing and/oradsorbing to the surface. In a non-limiting instance, the foulantforming components absorb onto the surface and do not adsorb onto thesurface; alternatively, the substance adsorbs onto the surface but doesnot absorb. The surface(s) may be or include, but are not limited to, ametal surface, a plastic surface, a ceramic surface, a painted surface,a coated surface, and combinations thereof. In a non-limitingembodiment, the metal surface may be or include steel, such as steelderived from iron, in a non-limiting example.

In a non-limiting embodiment, the foulant forming components may be orinclude metal carbonates, metal sulfates, metal oxides, metalphosphates, and combinations thereof. Alternatively, the foulant formingcomponents may be or include a metal, such as but not limited to,magnesium, calcium, barium, strontium, radium, iron, manganese, zinc,lead, cations thereof, and combinations thereof. Metal phosphates mayoccur when phosphorous containing compounds, e.g. orthophosphate, andthe metal are both present in a fluid and/or system. The retention ofthe respective salt constituents in ionic form, i.e. the solubility,depends upon such factors as water temperature, pH, ion concentration,and the like.

In a non-limiting embodiment, the protein(s) within the additivecomposition and/or fluid composition may be or include naturalprotein(s), recombinant protein(s), and combinations thereof. In anon-limiting embodiment, the protein(s) may include at least onechemical and/or biochemical modification, such as but not limited to atleast one label, at least one linker, at least one tag, and combinationsthereof.

The label may be or include, but is not limited to a radioactiveisotope, a fluorophore, an enzymatic label useful in tracing theprotein(s), and combinations thereof. The label or other modificationmay be useful in isolating the protein(s) from a specific bacteriumand/or other expression system (E. coli as described below). The labelor other modification may be used to identify the protein(s) once thefluid needs to be recovered, e.g. from a subterranean reservoirwellbore, refinery feed, and/or fluid composition.

A linker is a self-complementary oligomer that contains a recognitionsequence for a particular restriction enzyme. The restriction enzyme maycleave the linker from the amino acid sequence and generate ‘stickyends’ prior to cloning the protein(s). In a non-limiting embodiment, thelinker may be hydrophobic or hydrophilic.

The tag may be or include, but is not limited to, an affinity tag, asolubilization tag, a chromatography tag, and combinations thereof. Anaffinity tag may be added to a protein for better purification of theprotein from a biology source. Non-limiting examples of an affinity tagmay be or include a chitin binding protein (CBP), a maltose bindingprotein (MBP), a glutathione-S-transferase (GST), a polyhistidine tag,and combinations thereof.

The polyhistidine tag (also known as a ‘His-tag’, hexahistidine tag,6×His-tag, His6-tag, and the like) may be attached to a C-terminal endof the protein(s) in a non-limiting embodiment. A polyhistidine tag isan amino acid motif that may be attached to a protein(s), which has atleast six histidine (His) residues. Polyhistadine-tags may be used foraffinity purification of a polyhistidine-tagged recombinant protein(s)expressed in E. coli and/or other prokaryotic expression systems.

In a non-limiting embodiment, the polyhistidine-tag may enhance theability of the protein(s) to prevent, inhibit, and/or decrease foulantformation and/or foulant deposition. Although the inventors do not wishto be bound to a particular theory, it is believed that thepolyhistidine tag may have a strong affinity for divalent cations, sothe p polyhistidine tag may chelate Ba²⁺ or Ca²⁺ in solution in anon-limiting embodiment. Additionally, the carboxyl chemistry on thesurface of the protein(s) may chelate Ba²⁺ or Ca²⁺ in solution.Alternatively, because of the polyhistidine-tag's affinity for metalcompounds, the polyhistidine tag may attach or cluster on solid surfaces(e.g. pipes), thereby attaching the protein(s) to the surfaces, tofurther reduce or prevent foulant formation and/or foulant depositionthereon.

In a non-limiting embodiment, the solubilization tag may be used toassist the proper folding of the protein when expressed in achaperone-deficient species, such as E. coli. Non-limiting examples ofsolubilization tags may be or include, thioredoxin (TRX), poly(NANP),MBP, GST, and combinations thereof.

In a non-limiting embodiment, the chromatography tag may alterchromatographic properties of the protein for different resolutionsduring a particular separation technique. Such chromatography tags maybe or include, but are not limited to polyanionic amino acids.

To obtain the natural and/or recombinant protein(s), such protein(s) maybe purchased from a third party who specializes in isolating suchprotein(s) from a particular species and/or a third party whospecializes in recombinant generation of such protein(s). In anon-limiting embodiment, a bacteria that includes the protein(s) may beplated on a growth medium, such as an agar, which is conducive to thegrowth of the bacteria. The protein(s) may be directly isolated from thebacteria to be added to or used for decreasing foulant formation and/orfoulant deposition on a surface. ‘Isolated’ is defined herein to denotethat the protein(s) has been removed from the intact cells or cellulardebris, and is in a condition other than its native environment, is freeof other extraneous or unwanted nucleic acids, proteases, and lipids, ina form suitable for use as a protein(s) as described herein.

In a non-limiting embodiment, the protein(s) may be inserted into orjoined to a vector for insertion into a plasmid. A vector is a DNAmolecule that may be used as a vehicle to artificially carry geneticmaterial from a foreign cell and/or organism. A plasmid is defined as acircular extrachromosomal element found naturally in bacteria and someother organisms, which may be genetically engineered to clone DNAfragments. The plasmid may then be inserted into a host bacterium cell,such as Escherichia coli, where the host cell may replicate and/orexpress the foreign DNA. The E. coli cells may be plated on a growthmedium, such as an agar, which is conducive to the growth of E. coli.The growth of E. coli propagates the protein(s) as clones within each E.coli cell. The protein(s) may be isolated from the E. coli cells andsubsequently used as described herein. A non-limiting expression vectorhaving the protein(s) may be a commercially available pGS21 expressionvector, which is supplied by GenScript.

FIG. 4 represents a pGS21 plasmid for use as an expression vector for atleast one recombinant protein(s). The plasmid is depicted as having aHis tag, and a GST (Glutathione S Transferase) region, but such regionsare optional for purposes of cloning/expressing the protein(s) describedherein. The ‘Ampicillin’ region regulates the expression of β-lactamase;Ori is the DNA sequence that signals for the origin of replication (alsoknown as ‘origin’); lacI codes for the lactose repressor.

To isolate or obtain the protein(s) from E. coli, the E. coli cells maybe harvested via centrifugation to produce a cell pellet. The cellpellet may be lysed either by physical means or by chemical means, suchas detergents and/or enzymes (e.g. lysozyme) to produce a lysate. Theraw lysate may contain the recombinant protein, as well as otherproteins originating from the bacterial host. Thus, the raw lysatemixture may be incubated with an affinity resin having bound bivalentnickel and/or cobalt ions. The affinity resin may be sepharose/agarosefunctionalised with a chelator, such as but not limited to iminodiaceticacid (Ni-IDA), nitrilotriacetic acid (Ni-NTA), carboxylmethylaspartate(Co-CMA), and combinations thereof. The polyhistidine-tag may bind tothe affinity resin with micromolar affinity. The affinity resin with theattached polyhistidine-tag(s) may then be washed with a phosphate bufferto remove the protein(s) that do not bind thereto, while the proteinremains attached to the affinity resin via the polyhistidine tag. Thus,a polyhistidine tag allows the protein(s) to be purified in this manner.SDS-PAGE, Western blotting, and the like may be used to further assessthe purity and amount of purified protein(s).

The protein(s) may be in a powder form and/or a liquid form (e.g. insolution) when added to or included in the fluid composition. Theprotein(s) may be part of an additive where the additive includes theprotein(s), as well as other components to aid the protein(s) indecreasing foulant formation and/or foulant deposition.

The amount of the protein(s) within the additive composition may rangefrom about 0.01 wt % independently to about 10 wt % as compared to atotal base fluid, alternatively, from about 0.1 wt % independently toabout 8 wt %, or from about 1 wt % independently to about 5 wt % in anon-limiting embodiment.

In a non-limiting embodiment, the additive composition and/or fluidcomposition may include at least one additional component in an amountranging from about 1 ppm independently to about 10,000 ppm based on thetotal amount of the base fluid to be circulated at the same time ordifferent time as the additive composition. Alternatively, the amount ofthe additional component(s) within the additive composition may rangefrom about 100 ppm independently to about 5,000 ppm, or from about 1,000ppm independently to about 4,000 ppm.

In a non-limiting embodiment, the base fluid and/or fluid compositionmay include foulant forming components in an amount ranging from about10 ppm independently to about 50,000 ppm based on the total volume ofthe base fluid, alternatively from about 100 ppm independently to about25,000 ppm, or from about 1000 ppm independently to about 10,000 ppm.

The additional component(s) may be or include, but are not limited to,at least one scale inhibitor, at least one corrosion inhibitor,surfactants, biocides, demulsifiers, and combinations thereof.Non-limiting embodiments of the scale inhibitor(s) may be or include,but are not limited to, polyacrylates, polymaleates,hydroxypropylacrylates, phosphonates, polyphosphonates, soy proteinpolymers (e.g. Pre-Cote 5000 from DUPONT), polysaccharide basedinhibitors, polyaspartic acid based inhibitors, polymers thereof,copolymers thereof, and combinations thereof.

The additive composition may be added and/or included in a base fluid,such as but not limited to, an aqueous fluid, a non-aqueous fluid, anemulsified fluid, a non-emulsified fluid, and combinations thereof. In anon-limiting embodiment, the base fluid may be a drilling fluid, acompletion fluid, a production fluid, a servicing fluid, an injectionfluid, a refinery fluid, and combinations thereof to form a fluidcomposition. The pH of the base fluid, the additive composition, and/orthe fluid composition may be greater than about 3, alternatively fromabout 3 independently to about 9, or from about 5 independently to about7 in another non-limiting embodiment.

Moreover, the additive composition may contact a surface at the sametime or different time as the base fluid, i.e. the additive compositionmay contact the surface before, during, and/or after the base fluid. Ina non-limiting embodiment, the surface may be located in a downholesubterranean reservoir wellbore, a refinery, and combinations thereof.Said differently, the additive composition may be circulated into thelocation that includes the surface, such as a downhole subterraneanreservoir wellbore, a refinery, and combinations thereof before, during,and/or after the base fluid is circulated therein in a non-limitingembodiment.

In a non-limiting embodiment, the temperature of the additivecomposition and/or fluid composition and/or location of the surface mayrange from about 25° C. independently to about 200° C., alternativelyfrom about 70 C independently to about 175° C., or from about 100 Cindependently to about 150° C. in another non-limiting embodiment.

The contacting of the additive composition with the surface(s) maysuppress or decrease the amount of and/or the rate of foulant formationand/or foulant deposition to the surface(s). That is, it is notnecessary for foulant formation and/or foulant deposition to be entirelyprevented for the methods and compositions discussed herein to beconsidered effective, although complete prevention is a desirable goal.Success is obtained if less foulant formation and/or foulant depositionoccurs in the presence of the protein(s) than in the absence of theprotein(s). Alternatively, the methods and fluid compositions describedare considered successful if there is at least a 50% decrease in foulantdeposition and/or foulant formation on the targeted surfaces, such aswithin a subterranean wellbore and/or within a refinery.

Determination of the induction time for foulant formation and/or foulantdeposition in the presence or absence of the protein(s) may be used asan assay for the inhibition activity of the protein(s). Induction timemay be the time required for the onset point of the foulant formationand/or foulant deposition. The effect of a number of parametersincluding concentration of the protein(s), temperature, gas, and saltare determined and data subject to statistical analysis.

The growth rate of formed foulant(s) (e.g. precipitated foulants) in thepresence of the protein(s) may also be determined and compared toactivities of other protein(s) and/or known inhibitors for a particulartype of foulant. Effects of concentration of the protein(s),temperature, gas, and salt on the growth rate may also be examined.

‘Feed’ is defined herein to be a subterranean feed and/or a refineryfeed that includes a fluid and any components therein (e.g. pipes orconduits where the base fluid may flow through or alongside).

Circulating a base fluid and/or an additive composition into asubterranean reservoir wellbore and/or refinery may occur by injectingthe base fluid and/or the additive composition thereinto. The additivecomposition comprising the protein(s) may be circulated into thesubterranean reservoir wellbore and/or refinery feed at the same time ordifferent time as the base fluid (i.e. before, during, or after the basefluid). In the instance the protein(s) are circulated into thesubterranean reservoir wellbore and/or refinery at the same time as thebase fluid, the protein(s) may be added to the base fluid prior to thecirculation of the fluid composition into the subterranean reservoirwellbore or refinery in a non-limiting instance.

A drilling operation is used to drill into a subterranean reservoirformation, and a drilling fluid accompanies the drilling operation. Acompletions operation is performed to complete a well, such as theevents and assembly of equipment (e.g. downhole tubulars) to bring awell into production once the drilling operations are done. Astimulation operation is one where a treatment is performed to restoreor enhance the productivity of a well, such as hydraulic fracturing(above the fracture pressure of the reservoir formation) and matrixtreatments (below the fracture pressure of the reservoir formation). Aninjection operation includes a well where fluids are injected into thewell, instead of produced therefrom, to maintain reservoir pressuretherein. A servicing operation allows for maintenance to the well duringand/or after the well has been completed and/or produced, enhancing thewell productivity, and/or monitoring the performance of the well orreservoir.

Each downhole operation has its own respective downhole fluid, e.g.downhole operations utilize drilling fluids. Downhole fluids aretypically classified according to their base fluid. In aqueous basedfluids, solid particles are suspended in a continuous phase consistingof water or brine. Oil can be emulsified in the water, which is thecontinuous phase. “Aqueous based fluid” is used herein to include fluidshaving an aqueous continuous phase where the aqueous continuous phasecan be all water, brine, seawater, and combinations thereof; anoil-in-water emulsion, or an oil-in-brine emulsion; and combinationsthereof. For example, brine-based fluids are aqueous based fluids, inwhich the aqueous component is brine. ‘Brine’ is defined as awater-based fluid comprising salts that have been controllably addedthereto. ‘Seawater’ is similar to brine, but the salts in the seawaterhave been disposed therein by a natural process, e.g. ocean water is atype of seawater that formed in the absence of any man-madeintervention.

Non-aqueous base fluids are the opposite or inverse of aqueous-basedfluids. “Non-aqueous fluid” is used herein to include fluids having anon-aqueous continuous phase where the non-aqueous continuous phase isall oil, a non-aqueous fluid, a water-in-oil emulsion, awater-in-non-aqueous emulsion, a brine-in-oil emulsion, abrine-in-non-aqueous emulsion, a seawater-in-non-aqueous emulsion. Innon-aqueous-based fluids, solid particles are suspended in a continuousphase consisting of oil or another non-aqueous fluid. Water or brine canbe emulsified in the oil; therefore, the oil is the continuous phase. Inoil-based fluids, the oil may consist of any oil or water-immisciblefluid that may include, but is not limited to, diesel, mineral oil,esters, refinery cuts and blends, or alpha-olefins. Non-aqueous-basedfluid as defined herein may also include synthetic-based fluids or muds(SBMs), which are synthetically produced rather than refined fromnaturally-occurring materials. Synthetic-based fluids often include, butare not necessarily limited to, olefin oligomers of ethylene, estersmade from vegetable fatty acids and alcohols, ethers and polyethers madefrom alcohols and polyalcohols, paraffinic, or aromatic, hydrocarbonsalkyl benzenes, terpenes and other natural products and mixtures ofthese types.

In the foregoing specification, the invention has been described withreference to specific embodiments thereof, and has been described aseffective in providing additive compositions, fluid compositions, andmethods for decreasing foulant formation and/or foulant deposition on atleast one surface in contact with at least one protein. However, it willbe evident that various modifications and changes can be made theretowithout departing from the broader spirit or scope of the invention asset forth in the appended claims. Accordingly, the specification is tobe regarded in an illustrative rather than a restrictive sense. Forexample, specific base fluids, surfaces, proteins, scale formingcomponents, corrosion forming components, corrosion inhibitors, andscale inhibitors falling within the claimed parameters, but notspecifically identified or tried in a particular composition or method,are expected to be within the scope of this invention.

The present invention may suitably comprise, consist or consistessentially of the elements disclosed and may be practiced in theabsence of an element not disclosed. For instance, the additivecomposition for a base fluid, such as but not limited to, a drillingfluid, a completion fluid, a production fluid, a servicing fluid, aninjection fluid, a refinery fluid, and combinations thereof may consistof or consist essentially of at least one protein, such as but notlimited to, at least one aspein protein, at least one aspolin protein,at least one dentine protein, at least one DRICH-1 protein, at least onenacrein protein, at least one SMDT-1 protein, derivatives thereof,fragments thereof, mimetics thereof, and combinations thereof.

The fluid composition may consist of or consist essentially of a basefluid, at least one protein, and at least one foulant forming componentwhere less foulant formation occurs in the presence of the at least oneprotein as compared to an otherwise identical fluid composition absentthe at least one protein. The base fluid may be or include, but is notlimited to, aqueous-based fluids, non-aqueous-based fluids, emulsifiedfluids, non-emulsified fluids, and combinations thereof. The protein(s)may be or include, but is not limited to at least one aspein protein, atleast one aspolin protein, at least one dentine protein, at least oneDRICH-1 protein, at least one nacrein protein, an SMDT-1 protein,derivatives thereof, fragments thereof, mimetics thereof, andcombinations thereof.

The method may consist of or consist essentially of contacting at leastone surface with at least one protein, and decreasing an amount offoulant deposition onto the surface as compared to an otherwiseidentical surface absent the contact of the surface with the at leastone protein. The protein(s) may be or include, but are not limited to,at least one aspein protein, at least one aspolin protein, at least onedentine protein, at least one DRICH-1 protein, at least one nacreinprotein, at least one SMDT-1 protein, derivatives thereof, fragmentsthereof, mimetics thereof, and combinations thereof.

The words “comprising” and “comprises” as used throughout the claims,are to be interpreted to mean “including but not limited to” and“includes but not limited to”, respectively.

The invention claimed is:
 1. A method comprising: contacting at leastone surface with at least one protein selected from the group consistingof at least one aspein protein, at least one aspolin protein, at leastone dentine protein, at least one DRICH-1 protein, at least one nacreinprotein, at least one SMDT-1 protein, derivatives thereof, fragmentsthereof, mimetics thereof, and combinations thereof; and decreasing anamount of foulant deposition onto the at least one surface as comparedto an otherwise identical surface absent the contact of the at least onesurface with the at least one protein, where the foulant comprises atleast one member selected from the group consisting of metal carbonates,metal sulfates, metal oxides, and combinations thereof, and where themetal is selected from the group consisting of magnesium, calcium,barium, strontium, radium, iron, manganese, zinc, lead, cations thereof,and combinations thereof.
 2. The method of claim 1, wherein the at leastone protein is selected from the group consisting of at least one aspeinprotein and at least one aspolin protein, further wherein: the at leastone aspein protein comprises an amino acid sequence that is at least 75%homologous to the amino acid sequence of SEQ ID NO:1; the at least oneaspolin protein comprises an amino acid sequence that is at least 75%homologous to the amino acid SEQ ID:2, the amino acid SEQ ID:3, andcombinations thereof; and combinations thereof.
 3. The method of claim1, further comprising contacting the at least one surface with a basefluid before, during, or after contacting the at least one surface withthe at least one protein.
 4. The method of claim 3, wherein the fluidcomprises foulant forming components in an amount ranging from about 10ppm to about 50,000 ppm based on the total volume of the fluid beforecontacting the surface with the fluid.
 5. The method of claim 1 whereinthe at least one surface is at a location selected from the groupconsisting of a subterranean reservoir wellbore, a refinery feed, andcombinations thereof.
 6. The method of claim 3, wherein the base fluidis selected from the group consisting of aqueous-based fluids,non-aqueous-based fluids, emulsified fluids, non-emulsified fluids, andcombinations thereof.
 7. The method of claim 1, wherein the at least oneprotein is selected from the group consisting of natural proteins,recombinant proteins, and combinations thereof.
 8. The method of claim1, wherein the at least one protein comprises at least one modificationselected from the group consisting of a linker, a label, a tag, andcombinations thereof.
 9. The method of claim 1, wherein the method ispracticed at a temperature ranging from about 25° C. to about 200° C.10. A method comprising: contacting at least one surface with at leastone protein, wherein the at least one protein is selected from the groupconsisting of at least one aspein protein and at least one aspolinprotein, further wherein: the at least one aspein protein comprises anamino acid sequence that is at least 75% homologous to the amino acidsequence of SEQ ID NO:1; the at least one aspolin protein comprises anamino acid sequence that is at least 75% homologous to the amino acidSEQ ID:2, the amino acid SEQ ID:3, and combinations thereof; andcombinations thereof; decreasing an amount of foulant deposition ontothe at least one surface as compared to an otherwise identical surfaceabsent the contact of the at least one surface with the at least oneprotein, where the foulant comprises at least one member selected fromthe group consisting of metal carbonates, metal sulfates, metal oxides,and combinations thereof, and where the metal is selected from the groupconsisting of magnesium, calcium, barium, strontium, radium, iron,manganese, zinc, lead, cations thereof, and combinations thereof; andcontacting the at least one surface with a base fluid before, during, orafter contacting the at least one surface with the at least one protein,wherein the base fluid is selected from the group consisting ofaqueous-based fluids, non-aqueous-based fluids, emulsified fluids,non-emulsified fluids, and combinations thereof.
 11. The method of claim10, wherein the base fluid comprises foulant forming components in anamount ranging from about 10 ppm to about 50,000 ppm based on the totalvolume of the base fluid before contacting the surface with the fluid.12. The method of claim 10 wherein the at least one surface is at alocation selected from the group consisting of a subterranean reservoirwellbore, a refinery feed, and combinations thereof.
 13. The method ofclaim 10, wherein the at least one protein comprises at least onemodification selected from the group consisting of a linker, a label, atag, and combinations thereof.
 14. The method of claim 10, wherein themethod is practiced at a temperature ranging from about 25° C. to about200° C.
 15. A method comprising: contacting at least one surface with atleast one protein selected from the group consisting of at least oneaspein protein, at least one aspolin protein, at least one dentineprotein, at least one DRICH-1 protein, at least one nacrein protein, atleast one SMDT-1 protein, derivatives thereof, fragments thereof,mimetics thereof, and combinations thereof; decreasing an amount offoulant deposition onto the at least one surface as compared to anotherwise identical surface absent the contact of the at least onesurface with the at least one protein, wherein the foulant comprises atleast one member selected from the group consisting of metal carbonates,metal sulfates, metal oxides, and combinations thereof, where the metalis selected from the group consisting of magnesium, calcium, barium,strontium, radium, iron, manganese, zinc, lead, cations thereof, andcombinations thereof; and contacting the at least one surface with abase fluid before, during, or after contacting the at least one surfacewith the at least one protein.
 16. The method of claim 15, wherein theat least one protein is selected from the group consisting of at leastone aspein protein and at least one aspolin protein, further wherein:the at least one aspein protein comprises an amino acid sequence that isat least 75% homologous to the amino acid sequence of SEQ ID NO:1; theat least one aspolin protein comprises an amino acid sequence that is atleast 75% homologous to the amino acid SEQ ID:2, the amino acid SEQID:3, and combinations thereof; and combinations thereof.
 17. The methodof claim 15, wherein the base fluid comprises foulant forming componentsin an amount ranging from about 10 ppm to about 50,000 ppm based on thetotal volume of the fluid before contacting the surface with the fluid.18. The method of claim 15, wherein the method is practiced at atemperature ranging from about 25° C. to about 200° C.